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BDNF_PANTR
ID   BDNF_PANTR              Reviewed;         247 AA.
AC   Q5IS78;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Brain-derived neurotrophic factor;
DE            Short=BDNF;
DE   Contains:
DE     RecName: Full=BDNF precursor form {ECO:0000305};
DE              Short=ProBDNF {ECO:0000305};
DE   Flags: Precursor;
GN   Name=BDNF;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
CC   -!- FUNCTION: Important signaling molecule that activates signaling
CC       cascades downstream of NTRK2 (By similarity). During development,
CC       promotes the survival and differentiation of selected neuronal
CC       populations of the peripheral and central nervous systems. Participates
CC       in axonal growth, pathfinding and in the modulation of dendritic growth
CC       and morphology. Major regulator of synaptic transmission and plasticity
CC       at adult synapses in many regions of the CNS. The versatility of BDNF
CC       is emphasized by its contribution to a range of adaptive neuronal
CC       responses including long-term potentiation (LTP), long-term depression
CC       (LTD), certain forms of short-term synaptic plasticity, as well as
CC       homeostatic regulation of intrinsic neuronal excitability (By
CC       similarity). {ECO:0000250|UniProtKB:P21237,
CC       ECO:0000250|UniProtKB:P23560}.
CC   -!- FUNCTION: [BDNF precursor form]: Important signaling molecule that
CC       activates signaling cascades downstream of NTRK2. Activates signaling
CC       cascades via the heterodimeric receptor formed by NGFR and SORCS2.
CC       Signaling via NGFR and SORCS2 plays a role in synaptic plasticity and
CC       long-term depression (LTD). Binding to NGFR and SORCS2 promotes
CC       neuronal apoptosis. Promotes neuronal growth cone collapse.
CC       {ECO:0000250|UniProtKB:P21237}.
CC   -!- SUBUNIT: Monomers and homodimers (By similarity). Binds to NTRK2/TRKB.
CC       Can form heterodimers with other neurotrophin family members, such as
CC       NTF3 and NTF4 (in vitro), but the physiological relevance of this is
CC       not clear (By similarity). BDNF precursor form: interacts with the
CC       heterodimer formed by NGFR and SORCS2. Mature BDNF has much lower
CC       affinity for the heterodimer formed by NGFR and SORCS2 (By similarity).
CC       {ECO:0000250|UniProtKB:P21237, ECO:0000250|UniProtKB:P23560}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P23560}.
CC   -!- SUBCELLULAR LOCATION: [BDNF precursor form]: Secreted
CC       {ECO:0000250|UniProtKB:P23560}. Note=A proportion of BDNF is secreted
CC       as immature precursor (proBDNF). {ECO:0000250|UniProtKB:P23560}.
CC   -!- PTM: [BDNF precursor form]: N-glycosylated and glycosulfated, contrary
CC       to mature BDNF. {ECO:0000250|UniProtKB:P23560}.
CC   -!- PTM: Mature BDNF is produced by proteolytic removal of the propeptide,
CC       catalyzed by a FURIN family member. In addition, the precursor form is
CC       proteolytically cleaved within the propeptide, but this is not an
CC       obligatory intermediate for the production of mature BDNF. Can be
CC       converted into mature BDNF by plasmin (PLG).
CC       {ECO:0000250|UniProtKB:P23560}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   EMBL; AY665250; AAV74288.1; -; mRNA.
DR   RefSeq; NP_001012443.1; NM_001012441.1.
DR   AlphaFoldDB; Q5IS78; -.
DR   BMRB; Q5IS78; -.
DR   SMR; Q5IS78; -.
DR   STRING; 9598.ENSPTRP00000060385; -.
DR   PaxDb; Q5IS78; -.
DR   GeneID; 503511; -.
DR   KEGG; ptr:503511; -.
DR   CTD; 627; -.
DR   eggNOG; ENOG502QRU8; Eukaryota.
DR   HOGENOM; CLU_059942_0_0_1; -.
DR   InParanoid; Q5IS78; -.
DR   OrthoDB; 1156054at2759; -.
DR   TreeFam; TF106463; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0005163; F:nerve growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0007613; P:memory; IBA:GO_Central.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IBA:GO_Central.
DR   GO; GO:0021675; P:nerve development; IBA:GO_Central.
DR   GO; GO:0038180; P:nerve growth factor signaling pathway; IBA:GO_Central.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central.
DR   GO; GO:0048672; P:positive regulation of collateral sprouting; IBA:GO_Central.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR020430; Brain-der_neurotrophic_factor.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR020408; Nerve_growth_factor-like.
DR   InterPro; IPR002072; Nerve_growth_factor-rel.
DR   InterPro; IPR019846; Nerve_growth_factor_CS.
DR   PANTHER; PTHR11589; PTHR11589; 1.
DR   PANTHER; PTHR11589:SF3; PTHR11589:SF3; 1.
DR   Pfam; PF00243; NGF; 1.
DR   PIRSF; PIRSF001789; NGF; 1.
DR   PRINTS; PR01912; BDNFACTOR.
DR   PRINTS; PR00268; NGF.
DR   SMART; SM00140; NGF; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00248; NGF_1; 1.
DR   PROSITE; PS50270; NGF_2; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..247
FT                   /note="BDNF precursor form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000447537"
FT   PROPEP          19..128
FT                   /evidence="ECO:0000250|UniProtKB:P21237"
FT                   /id="PRO_0000019637"
FT   CHAIN           129..247
FT                   /note="Brain-derived neurotrophic factor"
FT                   /id="PRO_0000019638"
FT   SITE            57..58
FT                   /note="Cleavage; by MBTPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        141..208
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   DISULFID        186..237
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   DISULFID        196..239
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
SQ   SEQUENCE   247 AA;  27818 MW;  0A60488254722A99 CRC64;
     MTILFLTMVI SYFGCMKAAP MKEANIRGQG GLAYPGVRTH GTLESVNGPK AGSRGLTSLA
     DTFEHVIEEL LDEDQKVRPN EENNKDADLY TSRVMLSSQV PLEPPLLFLL EEYKNYLDAA
     NMSMRVRRHS DPARRGELSV CDSISEWVTA ADKKTAVDMS GGTVTVLEKV PVSKGQLKQY
     FYETKCNPMG YTKEGCRGID KRHWNSQCRT TQSYVRALTM DSKKRIGWRF IRIDTSCVCT
     LTIKRGR
 
 
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